Evidence map›Paper›PMID 29967541›Full record

ArticleNature structural & molecular biology2018

The role of tubulin-tubulin lattice contacts in the mechanism of microtubule dynamic instability.

Szymon W Manka, Carolyn A Moores

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 96 papers.

0numbers the graph read from it
0cells of the map it votes in
96citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

96 citing papers in PubMed.

  1. Review
  2. Article
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  5. Tubulin flux at spastin-induced nanodamage sites regulates microtubule rescue frequency and EB1 lifetimes.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  6. Review
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  8. Article
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  18. Mechanisms of microtubule dynamics from single-molecule measurements.bioRxiv : the preprint server for biology · 2025
    Article
  19. Microtubule dynamics are defined by conformations and stability of clustered protofilaments.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  20. Article

36 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

Szymon W MankaInstitute of Structural and Molecular Biology, Department of Biological Sciences, Birkbeck, University of London, London, UK. s.manka@mail.cryst.bbk.ac.uk.ORCID 0000-0001-6733-146X
Carolyn A MooresInstitute of Structural and Molecular Biology, Department of Biological Sciences, Birkbeck, University of London, London, UK. c.moores@mail.cryst.bbk.ac.uk.ORCID 0000-0001-5686-6290

Funding

Medical Research Council MR/J000973/1Medical Research Council MR/R000352/1
6 · The paper itself

Abstract

Microtubules form from longitudinally and laterally assembling tubulin α-β dimers. The assembly induces strain in tubulin, resulting in cycles of microtubule catastrophe and regrowth. This 'dynamic instability' is governed by GTP hydrolysis that renders the microtubule lattice unstable, but it is unclear how. We used a human microtubule nucleating and stabilizing neuronal protein, doublecortin, and high-resolution cryo-EM to capture tubulin's elusive hydrolysis intermediate GDP•Pi state, alongside the prehydrolysis analog GMPCPP state and the posthydrolysis GDP state with and without an anticancer drug, Taxol. GTP hydrolysis to GDP•Pi followed by Pi release constitutes two distinct structural transitions, causing unevenly distributed compressions of tubulin dimers, thereby tightening longitudinal and loosening lateral interdimer contacts. We conclude that microtubule catastrophe is triggered because the lateral contacts can no longer counteract the strain energy stored in the lattice, while reinforcement of the longitudinal contacts may support generation of force.

Indexed as

Biophysical PhenomenaCryoelectron MicroscopyDoublecortin Domain ProteinsGTP PhosphohydrolasesGuanine NucleotidesHumansMicrotubule-Associated ProteinsMicrotubulesModels, BiologicalModels, MolecularNeuropeptidesProtein Interaction Domains and MotifsProtein MultimerizationProtein StabilityTubulinDoublecortin Domain ProteinsGTP PhosphohydrolasesGuanine NucleotidesMicrotubule-Associated ProteinsNeuropeptidesTubulin

Identifiers

PMID29967541
PMCPMC6201834

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.